| Reference |
Rout MP, Aitchison JD, Suprapto A, Hjertaas K, Zhao Y, Chait BT. The yeast nuclear pore complex: composition, architecture, and transport mechanism. J Cell Biol. 2000 Feb 21 148(4):635-51. p.644 right column 2nd paragraphPubMed ID10684247
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| Comments |
This indicates a surprisingly
simple composition for such a massive structure (e.g.,
given
~75 different proteins in a ribosome), and is significantly
lower than previous estimates (Rout and Wente, 1994). For value of ~30 different proteins to make up npc see Khmelinskii et al., 2012 PMID 22729030 p.709 right column 4th paragraph: "Each NPC [eukaryotic organism unspecified] comprises ~30 different proteins, called nucleoporins, that form pores in the nuclear envelope and control nucleocytoplasmic transport and nuclear organization (Fig. 3a). In organisms with open mitosis, NPCs disassemble when the nuclear envelope breaks down during cell division but are stable in nondividing cells." See Yang et al., 2017 PMID 28446921 p.1 2nd paragraph: "The nuclear pore complex (NPC) is the gateway of macromolecular trafficking between the nucleus and the cytoplasm (Xu and Meier, 2008). Being one of the largest multi-protein complexes in the
cell, the NPC consists of multiple copies of ~30 different proteins known as nucleoporins (Nups), which are organized in an octagonal manner and symmetrically around the cylindrical axis of the NPC (Alber et al., 2007, Tamura et al., 2010, Tamura and Hara-Nishimura, 2013)." |